2ab6: Difference between revisions

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New page: left|200px<br /> <applet load="2ab6" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ab6, resolution 2.50Å" /> '''HUMAN GLUTATHIONE S...
 
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[[Image:2ab6.gif|left|200px]]<br />
[[Image:2ab6.gif|left|200px]]<br /><applet load="2ab6" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2ab6" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2ab6, resolution 2.50&Aring;" />
caption="2ab6, resolution 2.50&Aring;" />
'''HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18) complexed with S-METHYLGLUTATHIONE'''<br />
'''HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18) complexed with S-METHYLGLUTATHIONE'''<br />


==Overview==
==Overview==
Human glutathione-S-transferase M2-2 (hGSTM2-2) was expressed in, Escherichia coli and purified by GSH-affinity chromatography. The, recombinant enzyme and the protein isolated from human tissue were, indistinguishable based on physicochemical, enzymatic and immunological, criteria. The catalytically active dimeric hGSTM2-2 was crystallized, without GSH or other active-site ligands in two crystal forms. Diffraction, from form A crystals extends to 2.5 A and is consistent with the space, group P21 (a = 53.9, b = 81.5, c = 55.6 A, beta = 109.26 A) with two, monomers in the asymmetric unit. Diffraction from form B crystals extends, to 3 A and is consistent with a space group P212121 (a = 57.2, b = 80.7, c, = 225.9 A) with two dimers in the asymmetric unit. This is the first, report of ligand-free mu-class GST crystals, and a comparison with, liganded complexes will provide insight into the structural consequences, of substrate binding which are thought to be important for catalysis.
Human glutathione-S-transferase M2-2 (hGSTM2-2) was expressed in Escherichia coli and purified by GSH-affinity chromatography. The recombinant enzyme and the protein isolated from human tissue were indistinguishable based on physicochemical, enzymatic and immunological criteria. The catalytically active dimeric hGSTM2-2 was crystallized without GSH or other active-site ligands in two crystal forms. Diffraction from form A crystals extends to 2.5 A and is consistent with the space group P21 (a = 53.9, b = 81.5, c = 55.6 A, beta = 109.26 A) with two monomers in the asymmetric unit. Diffraction from form B crystals extends to 3 A and is consistent with a space group P212121 (a = 57.2, b = 80.7, c = 225.9 A) with two dimers in the asymmetric unit. This is the first report of ligand-free mu-class GST crystals, and a comparison with liganded complexes will provide insight into the structural consequences of substrate binding which are thought to be important for catalysis.


==About this Structure==
==About this Structure==
2AB6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with GSM as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AB6 OCA].  
2AB6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=GSM:'>GSM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AB6 OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Almo, S.C.]]
[[Category: Almo, S C.]]
[[Category: Listowsky, I.]]
[[Category: Listowsky, I.]]
[[Category: Patskovsky, Y.]]
[[Category: Patskovsky, Y.]]
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[[Category: transferase]]
[[Category: transferase]]


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